GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network

Luke, M. R., Kjer-Nielsen, L., Brown, D. L., Stow, J. L. and Gleeson, P. A. (2003) GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. Journal of Biological Chemistry, 278 6: 4216-4226. doi:10.1074/jbc.M210387200

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Author Luke, M. R.
Kjer-Nielsen, L.
Brown, D. L.
Stow, J. L.
Gleeson, P. A.
Title GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2003-01-01
Year available 2003
Sub-type Article (original research)
DOI 10.1074/jbc.M210387200
Open Access Status File (Publisher version)
Volume 278
Issue 6
Start page 4216
End page 4226
Total pages 11
Editor Herbert Tabor
Place of publication Bethesda, USA
Publisher American Society for Biochemistry and Molecular Biology, Inc.
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780106 Political science and public policy
Abstract The GRIP domain is a targeting sequence found in a family of coiled-coil peripheral Golgi proteins. Previously we demonstrated that the GRIP domain of p230/golgin245 is specifically recruited to tubulovesicular structures of the traps-Golgi network (TGN). Here we have characterized two novel Golgi proteins with functional GRIP domains, designated GCC88 and GCC185. GCC88 cDNA encodes a protein of 88 kDa, and GCC185 cDNA encodes a protein of 185 kDa. Both molecules are brefeldin A-sensitive peripheral membrane proteins and are predicted to have extensive coiled-coil regions with the GRIP domain at the C terminus. By immunofluorescence and immunoelectron microscopy GCC88 and GCC185, and the GRIP protein golgin97, are all localized to the TGN of Hela cells. Overexpression of full-length GCC88 leads to the formation of large electron dense structures that extend from the traps-Golgi. These de novo structures contain GCC88 and co-stain for the TGN markers syntaxin 6 and TGN38 but not for alpha2,6-sialyltransferase, beta-COP, or cis-Golgi GM130. The formation of these abnormal structures requires the N-terminal domain of GCC88. TGN38, which recycles between the TGN and plasma membrane, was transported into and out of the GCC88 decorated structures. These data introduce two new GRIP domain proteins and implicate a role for GCC88 in the organization of a specific TGN subcompartment involved with membrane transport.
Keyword Biochemistry & Molecular Biology
Complex
Apparatus
Sequence
Insights
P230
Ypt6
Q-Index Code C1
Institutional Status UQ

 
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Created: Wed, 15 Aug 2007, 11:33:18 EST